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Literature summary for 1.8.1.B1 extracted from

  • Kalita, P.; Shukla, H.; Gadhave, K.; Giri, R.; Tripathi, T.
    Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase (2018), Arch. Biochem. Biophys., 656, 38-45 .
    View publication on PubMed
Search for more literature for 1.8.1.B1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Fasciola gigantica

General Stability

General Stability Organism
activities Fasciola gigantica
the Grx domain stabilizes the full-length FgTGRsec protein for efficient catalysis Fasciola gigantica
the urea-induced unfolding of the recombinant enzyme (FgTGRsec) and its N-terminal truncated variant (DELTANTDFgTGRsec) undergo unfolding in a three state manner. First, the protein undergoes a conformational transition rendering a near-native state with no FAD bound, and then full unfolding of the apodimer occurs without dissociation. The Grx domain stabilizes the global FgTGRsec structure and positively regulates FgTGRsec activity, and alteration in the FAD microenvironment is directly proportional to the loss of thioredoxin reductase (TrxR) and glutathione reductase Fasciola gigantica

Metals/Ions

Metals/Ions Comment Organism Structure
selenium role of selenocysteine in maintaining structure-function Fasciola gigantica

Organism

Organism UniProt Comment Textmining
Fasciola gigantica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Fasciola gigantica

Synonyms

Synonyms Comment Organism
TGRsec
-
 Fasciola gigantica
thioredoxin glutathione reductase
-
 Fasciola gigantica

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Fasciola gigantica

General Information

General Information Comment Organism
physiological function the enzyme plays a principal role in redox homeostasis maintenance Fasciola gigantica